Objective: To clone the influenza A virus NP gene into expression vector and to purify the target protein, which was used to study the preparation of monoclonal antibody.
Methods: The RNA of influenza A virus was extracted and primers were designed according the NP gene sequence, then the NP gene of influenza A virus was expressed in E.coli DH5alpha and the NP protein was purified by affinity chromatography.
Results: The recombinant expression vector-pGEX-4T-2-NP was successfully constructed and relatively pure target protein was obtained.
Conclusion: Through reasonably controlling the fermentation time, growth temperature and induction concentration, satisfactory soluble target product was obtained.
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